The mechanism ofT. cruziFPPS involves a substrate induced conformational change
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چکیده
منابع مشابه
Substrate-induced conformational change in a trimeric ornithine transcarbamoylase.
The crystal structure of Escherichia coli ornithine transcarbamoylase (OTCase, EC 2.1.3.3) complexed with the bisubstrate analog N-(phosphonacetyl)-L-ornithine (PALO) has been determined at 2.8-A resolution. This research on the structure of a transcarbamoylase catalytic trimer with a substrate analog bound provides new insights into the linkages between substrate binding, protein-protein inter...
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Carbohydrate-binding proteins occur widely in the plant kingdom. These proteins, commonly derived from seeds, are called phytohemagglutiuins or lectins (reviewed by Sharon and Lis’). It has become increasingly apparent that lectins can serve as probes for carbohydrate structure and function. The jack-bean lectin, namely, concanavalin A (con A), has received considerable attention because of its...
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Active transport of substrates across cytoplasmic membranes is of great physiological, medical and pharmaceutical importance. The glycerol-3-phosphate (G3P) transporter (GlpT) of the E. coli inner membrane is a secondary active antiporter from the ubiquitous major facilitator superfamily that couples the import of G3P to the efflux of inorganic phosphate (P(i)) down its concentration gradient. ...
متن کاملTransport properties of the galactose-binding protein of Escherichia coli. Substrate-induced conformational change.
The galactose-binding protein, a necessary component of a bacterical transport system, is shown by three independent methods to undergo a conformational change upon binding of substrate. 1. A Lineweaver-Burk plot of the binding data obtained by equilibrium dialysis at a protein concentration of 0.4 mg per ml shows heterogenous behavior. Extrapolation of the data at low galactose concentrations ...
متن کاملTransition States: Substrate- induced Conformational Transitions
In eqn [1], E is the stable formof the enzyme in the free state and Eact is the conformation of the enzyme stabilized by interaction with the substrate S; P represents the reaction product. The structure Eact is more complementary to the substrate than is E and thus is the more catalytically active form.Changes in the conformationof an enzymeas a result of substrate binding might be anticipated...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305091610